PIM1_HUMAN
ID PIM1_HUMAN Reviewed; 313 AA.
AC P11309; Q38RT9; Q5T7H7; Q96RG3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 4.
DT 03-AUG-2022, entry version 246.
DE RecName: Full=Serine/threonine-protein kinase pim-1;
DE EC=2.7.11.1;
GN Name=PIM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2205533; DOI=10.1016/0378-1119(90)90195-w;
RA Reeves R., Spies G.A., Kiefer M., Barr P.J., Power M.;
RT "Primary structure of the putative human oncogene, pim-1.";
RL Gene 90:303-307(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3475233; DOI=10.1016/0378-1119(87)90352-0;
RA Zakut-Houri R., Hazum S., Givol D., Telerman A.;
RT "The cDNA sequence and gene analysis of the human pim oncogene.";
RL Gene 54:105-111(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3329709;
RA Domen J., von Lindern M., Hermans A., Breuer M., Grosveld G., Berns A.;
RT "Comparison of the human and mouse PIM-1 cDNAs: nucleotide sequence and
RT immunological identification of the in vitro synthesized PIM-1 protein.";
RL Oncogene Res. 1:103-112(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3429489; DOI=10.1002/jcb.240350204;
RA Meeker T.C., Nagarajan L., Ar-Rushdi A., Croce C.M.;
RT "Cloning and characterization of the human PIM-1 gene: a putative oncogene
RT related to the protein kinases.";
RL J. Cell. Biochem. 35:105-112(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE INITIATION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH BMX.
RX PubMed=16186805; DOI=10.1038/sj.onc.1209058;
RA Xie Y., Xu K., Dai B., Guo Z., Jiang T., Chen H., Qiu Y.;
RT "The 44 kDa Pim-1 kinase directly interacts with tyrosine kinase Etk/BMX
RT and protects human prostate cancer cells from apoptosis induced by
RT chemotherapeutic drugs.";
RL Oncogene 25:70-78(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-202 (ISOFORM 1).
RX PubMed=11460166; DOI=10.1038/35085588;
RA Pasqualucci L., Neumeister P., Goossens T., Nanjangud G., Chaganti R.S.K.,
RA Kuppers R., Dalla-Favera R.;
RT "Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell
RT lymphomas.";
RL Nature 412:341-346(2001).
RN [10]
RP CHARACTERIZATION.
RX PubMed=2837645; DOI=10.1128/mcb.8.4.1498-1503.1988;
RA Telerman A., Amson R., Zakut-Houri R., Givol D.;
RT "Identification of the human pim-1 gene product as a 33-kilodalton
RT cytoplasmic protein with tyrosine kinase activity.";
RL Mol. Cell. Biol. 8:1498-1503(1988).
RN [11]
RP FUNCTION, AND ALTERNATIVE INITIATION.
RX PubMed=1825810; DOI=10.1002/j.1460-2075.1991.tb07994.x;
RA Saris C.J., Domen J., Berns A.;
RT "The pim-1 oncogene encodes two related protein-serine/threonine kinases by
RT alternative initiation at AUG and CUG.";
RL EMBO J. 10:655-664(1991).
RN [12]
RP INTERACTION WITH CBX3, AND FUNCTION IN PHOSPHORYLATION OF CBX3.
RX PubMed=10664448; DOI=10.1016/s0014-5793(00)01105-4;
RA Koike N., Maita H., Taira T., Ariga H., Iguchi-Ariga S.M.M.;
RT "Identification of heterochromatin protein 1 (HP1) as a phosphorylation
RT target by Pim-1 kinase and the effect of phosphorylation on the
RT transcriptional repression function of HP1.";
RL FEBS Lett. 467:17-21(2000).
RN [13]
RP SUBCELLULAR LOCATION, FUNCTION IN PHOSPHORYLATION OF CDKN1A, AND
RP INTERACTION WITH CDKN1A.
RX PubMed=12431783; DOI=10.1016/s0167-4889(02)00347-6;
RA Wang Z., Bhattacharya N., Mixter P.F., Wei W., Sedivy J., Magnuson N.S.;
RT "Phosphorylation of the cell cycle inhibitor p21Cip1/WAF1 by Pim-1
RT kinase.";
RL Biochim. Biophys. Acta 1593:45-55(2002).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=12680209;
RA Ionov Y., Le X., Tunquist B.J., Sweetenham J., Sachs T., Ryder J.,
RA Johnson T., Lilly M.B., Kraft A.S.;
RT "Pim-1 protein kinase is nuclear in Burkitt's lymphoma: nuclear
RT localization is necessary for its biologic effects.";
RL Anticancer Res. 23:167-178(2003).
RN [15]
RP INTERACTION WITH PPP2CA, PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=12473674; DOI=10.1074/jbc.m208246200;
RA Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.;
RT "Protein phosphatase 2A regulates the stability of Pim protein kinases.";
RL J. Biol. Chem. 278:4800-4805(2003).
RN [16]
RP FUNCTION, AND INDUCTION.
RX PubMed=15528381; DOI=10.4049/jimmunol.173.10.6409;
RA Stout B.A., Bates M.E., Liu L.Y., Farrington N.N., Bertics P.J.;
RT "IL-5 and granulocyte-macrophage colony-stimulating factor activate STAT3
RT and STAT5 and promote Pim-1 and cyclin D3 protein expression in human
RT eosinophils.";
RL J. Immunol. 173:6409-6417(2004).
RN [17]
RP UBIQUITINATION, INTERACTION WITH HSP90AA1 AND HSP70, AND INDUCTION.
RX PubMed=15798097; DOI=10.1158/1541-7786.mcr-04-0192;
RA Shay K.P., Wang Z., Xing P.X., McKenzie I.F., Magnuson N.S.;
RT "Pim-1 kinase stability is regulated by heat shock proteins and the
RT ubiquitin-proteasome pathway.";
RL Mol. Cancer Res. 3:170-181(2005).
RN [18]
RP FUNCTION IN PHOSPHORYLATION OF CDC25C, AND INTERACTION WITH CDC25C.
RX PubMed=16356754; DOI=10.1016/j.biocel.2005.10.010;
RA Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.;
RT "The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and
RT activates the G2/M specific phosphatase Cdc25C.";
RL Int. J. Biochem. Cell Biol. 38:430-443(2006).
RN [19]
RP FUNCTION IN CELL CYCLE PROGRESSION, INTERACTION WITH CDKN1B AND FOXO3, AND
RP PHOSPHORYLATION OF CDKN1B AND FOXO3.
RX PubMed=18593906; DOI=10.1158/0008-5472.can-08-0634;
RA Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.;
RT "Pim kinases promote cell cycle progression by phosphorylating and down-
RT regulating p27Kip1 at the transcriptional and posttranscriptional levels.";
RL Cancer Res. 68:5076-5085(2008).
RN [20]
RP FUNCTION.
RX PubMed=18056989; DOI=10.1074/jbc.m707773200;
RA Xie Y., Xu K., Linn D.E., Yang X., Guo Z., Shimelis H., Nakanishi T.,
RA Ross D.D., Chen H., Fazli L., Gleave M.E., Qiu Y.;
RT "The 44-kDa Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its
RT multimerization and drug-resistant activity in human prostate cancer
RT cells.";
RL J. Biol. Chem. 283:3349-3356(2008).
RN [21]
RP FUNCTION IN PHOSPHORYLATION OF MAP3K5, AND INTERACTION WITH MAP3K5.
RX PubMed=19749799; DOI=10.1038/onc.2009.276;
RA Gu J.J., Wang Z., Reeves R., Magnuson N.S.;
RT "PIM1 phosphorylates and negatively regulates ASK1-mediated apoptosis.";
RL Oncogene 28:4261-4271(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 33-305 IN COMPLEXES WITH
RP ADENOSINE AND INHIBITORS STAUROSPORINE AND LY294002, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT SER-8; THR-23; SER-98 AND SER-261.
RX PubMed=15657054; DOI=10.1074/jbc.m413155200;
RA Jacobs M.D., Black J., Futer O., Swenson L., Hare B., Fleming M.,
RA Saxena K.;
RT "Pim-1 ligand-bound structures reveal the mechanism of serine/threonine
RT kinase inhibition by LY294002.";
RL J. Biol. Chem. 280:13728-13734(2005).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 14-313 OF APOPROTEIN AND IN
RP COMPLEX WITH AMP-PNP, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY
RP REGULATION.
RX PubMed=15525646; DOI=10.1074/jbc.m409123200;
RA Qian K.C., Wang L., Hickey E.R., Studts J., Barringer K., Peng C.,
RA Kronkaitis A., Li J., White A., Mische S., Farmer B.;
RT "Structural basis of constitutive activity and a unique nucleotide binding
RT mode of human Pim-1 kinase.";
RL J. Biol. Chem. 280:6130-6137(2005).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-313 OF APOPROTEIN AND IN
RP COMPLEXES WITH AMP-PNP AND INHIBITORS, PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, COFACTOR, AND MUTAGENESIS OF HIS-68; PRO-81;
RP ASN-82 AND LEU-193.
RX PubMed=15808862; DOI=10.1016/j.jmb.2005.02.039;
RA Kumar A., Mandiyan V., Suzuki Y., Zhang C., Rice J., Tsai J., Artis D.R.,
RA Ibrahim P., Bremer R.;
RT "Crystal structures of proto-oncogene kinase Pim1: a target of aberrant
RT somatic hypermutations in diffuse large cell lymphoma.";
RL J. Mol. Biol. 348:183-193(2005).
RN [26]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-53; GLN-124; LYS-135 AND ASP-142.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity involved
CC in cell survival and cell proliferation and thus providing a selective
CC advantage in tumorigenesis. Exerts its oncogenic activity through: the
CC regulation of MYC transcriptional activity, the regulation of cell
CC cycle progression and by phosphorylation and inhibition of proapoptotic
CC proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an
CC increase of MYC protein stability and thereby an increase of
CC transcriptional activity. The stabilization of MYC exerted by PIM1
CC might explain partly the strong synergism between these two oncogenes
CC in tumorigenesis. Mediates survival signaling through phosphorylation
CC of BAD, which induces release of the anti-apoptotic protein Bcl-
CC X(L)/BCL2L1. Phosphorylation of MAP3K5, another proapoptotic protein,
CC by PIM1, significantly decreases MAP3K5 kinase activity and inhibits
CC MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently
CC reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle
CC progression at the G1-S and G2-M transitions by phosphorylation of
CC CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle
CC progression at G1, results in the relocation of CDKN1A to the cytoplasm
CC and enhanced CDKN1A protein stability. Promotes cell cycle progression
CC and tumorigenesis by down-regulating expression of a regulator of cell
CC cycle progression, CDKN1B, at both transcriptional and post-
CC translational levels. Phosphorylation of CDKN1B, induces 14-3-3
CC proteins binding, nuclear export and proteasome-dependent degradation.
CC May affect the structure or silencing of chromatin by phosphorylating
CC HP1 gamma/CBX3. Acts also as a regulator of homing and migration of
CC bone marrow cells involving functional interaction with the CXCL12-
CC CXCR4 signaling axis. Also phosphorylates and activates the ATP-binding
CC cassette transporter ABCG2, allowing resistance to drugs through their
CC excretion from cells (PubMed:18056989). Promotes brown adipocyte
CC differentiation (By similarity). {ECO:0000250|UniProtKB:P06803,
CC ECO:0000269|PubMed:10664448, ECO:0000269|PubMed:12431783,
CC ECO:0000269|PubMed:15528381, ECO:0000269|PubMed:16356754,
CC ECO:0000269|PubMed:18056989, ECO:0000269|PubMed:1825810,
CC ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:19749799}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:15525646, ECO:0000269|PubMed:15657054,
CC ECO:0000269|PubMed:15808862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15525646,
CC ECO:0000269|PubMed:15657054, ECO:0000269|PubMed:15808862};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15525646, ECO:0000269|PubMed:15657054,
CC ECO:0000269|PubMed:15808862};
CC -!- SUBUNIT: Isoform 1 is isolated as a monomer whereas isoform 2 complexes
CC with other proteins (By similarity). Binds to RP9 (By similarity).
CC Isoform 2, but not isoform 1, binds BMX (PubMed:16186805). Isoform 1
CC interacts with CDKN1B and FOXO3 (PubMed:18593906). Interacts with BAD
CC (By similarity). Interacts with PPP2CA; this interaction promotes
CC dephosphorylation of PIM1, ubiquitination and proteasomal degradation
CC (PubMed:12473674). Interacts with HSP90AA1, this interaction stabilizes
CC PIM1 protein levels. Interacts (ubiquitinated form) with HSP70 and
CC promotes its proteosomal degradation (PubMed:15798097). Interacts with
CC CDKN1A (PubMed:12431783). Interacts with CDC25C (PubMed:16356754).
CC Interacts (via N-terminal 96 residues) with CDC25A (By similarity).
CC Interacts with MAP3K5 (PubMed:19749799). Interacts with MYC (By
CC similarity). Interacts with CBX3 (PubMed:10664448).
CC {ECO:0000250|UniProtKB:P06803, ECO:0000269|PubMed:10664448,
CC ECO:0000269|PubMed:12431783, ECO:0000269|PubMed:12473674,
CC ECO:0000269|PubMed:15798097, ECO:0000269|PubMed:16186805,
CC ECO:0000269|PubMed:16356754, ECO:0000269|PubMed:18593906,
CC ECO:0000269|PubMed:19749799}.
CC -!- INTERACTION:
CC P11309; Q8N9N5: BANP; NbExp=3; IntAct=EBI-696621, EBI-744695;
CC P11309; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-696621, EBI-10181188;
CC P11309; P51813: BMX; NbExp=2; IntAct=EBI-696621, EBI-696657;
CC P11309; P07954: FH; NbExp=3; IntAct=EBI-696621, EBI-1050358;
CC P11309; P51116: FXR2; NbExp=3; IntAct=EBI-696621, EBI-740459;
CC P11309; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-696621, EBI-5460660;
CC P11309; Q5T203: NHLH1; NbExp=3; IntAct=EBI-696621, EBI-10197511;
CC P11309; P39019: RPS19; NbExp=7; IntAct=EBI-696621, EBI-354451;
CC P11309; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-696621, EBI-10178002;
CC P11309; Q9Y2K1: ZBTB1; NbExp=3; IntAct=EBI-696621, EBI-2682961;
CC P11309-1; P46527: CDKN1B; NbExp=2; IntAct=EBI-1018629, EBI-519280;
CC P11309-1; O43524: FOXO3; NbExp=2; IntAct=EBI-1018629, EBI-1644164;
CC P11309-1; Q9BZS1-1: FOXP3; NbExp=3; IntAct=EBI-1018629, EBI-9695448;
CC P11309-2; Q9UNQ0: ABCG2; NbExp=5; IntAct=EBI-1018633, EBI-1569435;
CC P11309-2; P51813: BMX; NbExp=6; IntAct=EBI-1018633, EBI-696657;
CC P11309-2; P17252: PRKCA; NbExp=2; IntAct=EBI-1018633, EBI-1383528;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=Pim-1 {ECO:0000303|PubMed:18056989};
CC IsoId=P11309-1; Sequence=Displayed;
CC Name=2; Synonyms=Pim-1L {ECO:0000303|PubMed:18056989};
CC IsoId=P11309-2; Sequence=VSP_059829;
CC -!- TISSUE SPECIFICITY: Expressed primarily in cells of the hematopoietic
CC and germline lineages. Isoform 1 and isoform 2 are both expressed in
CC prostate cancer cell lines. {ECO:0000269|PubMed:16186805}.
CC -!- INDUCTION: Strongly induced in leukocytes by the JAK/STAT pathway in
CC response to cytokines. Induced by different cellular stresses, heat
CC shock and cytotoxic agents. {ECO:0000269|PubMed:15528381,
CC ECO:0000269|PubMed:15798097, ECO:0000269|PubMed:16186805}.
CC -!- PTM: Autophosphorylated on both serine/threonine and tyrosine residues.
CC Phosphorylated. Interaction with PPP2CA promotes dephosphorylation.
CC {ECO:0000269|PubMed:12473674, ECO:0000269|PubMed:15657054,
CC ECO:0000269|PubMed:18593906}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000269|PubMed:12473674, ECO:0000269|PubMed:15798097}.
CC -!- MISCELLANEOUS: [Isoform 2]: Initiates from CTG codon.
CC {ECO:0000269|PubMed:16186805, ECO:0000269|PubMed:1825810}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PIM subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PIM1ID261.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M27903; AAA60090.1; -; Genomic_DNA.
DR EMBL; M16750; AAA60089.1; -; mRNA.
DR EMBL; M54915; AAA36447.1; -; mRNA.
DR EMBL; M24779; AAA81553.1; -; mRNA.
DR EMBL; DQ022562; AAY87461.1; -; mRNA.
DR EMBL; AL353579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03934.1; -; Genomic_DNA.
DR EMBL; BC020224; AAH20224.1; -; mRNA.
DR EMBL; AF386792; AAK70871.1; -; Genomic_DNA.
DR CCDS; CCDS4830.1; -. [P11309-1]
DR PIR; JU0327; TVHUP1.
DR RefSeq; NP_001230115.1; NM_001243186.1. [P11309-2]
DR RefSeq; NP_002639.1; NM_002648.3. [P11309-1]
DR PDB; 1XQZ; X-ray; 2.10 A; A=14-313.
DR PDB; 1XR1; X-ray; 2.10 A; A=14-313.
DR PDB; 1XWS; X-ray; 1.80 A; A=1-313.
DR PDB; 1YHS; X-ray; 2.15 A; A=33-305.
DR PDB; 1YI3; X-ray; 2.50 A; A=33-305.
DR PDB; 1YI4; X-ray; 2.40 A; A=33-305.
DR PDB; 1YWV; X-ray; 2.00 A; A=29-313.
DR PDB; 1YXS; X-ray; 2.20 A; A=29-313.
DR PDB; 1YXT; X-ray; 2.00 A; A=29-313.
DR PDB; 1YXU; X-ray; 2.24 A; A/B/C/D=29-313.
DR PDB; 1YXV; X-ray; 2.00 A; A=29-313.
DR PDB; 1YXX; X-ray; 2.00 A; A=29-313.
DR PDB; 2BIK; X-ray; 1.80 A; B=1-313.
DR PDB; 2BIL; X-ray; 2.55 A; B=1-313.
DR PDB; 2BZH; X-ray; 1.90 A; B=1-313.
DR PDB; 2BZI; X-ray; 1.90 A; B=1-313.
DR PDB; 2BZJ; X-ray; 2.05 A; A=1-313.
DR PDB; 2BZK; X-ray; 2.45 A; B=1-313.
DR PDB; 2C3I; X-ray; 1.90 A; B=1-313.
DR PDB; 2J2I; X-ray; 1.90 A; B=1-312.
DR PDB; 2O3P; X-ray; 2.24 A; A=29-313.
DR PDB; 2O63; X-ray; 2.00 A; A=29-313.
DR PDB; 2O64; X-ray; 2.44 A; A=29-313.
DR PDB; 2O65; X-ray; 2.85 A; A=29-313.
DR PDB; 2OBJ; X-ray; 2.50 A; A=1-313.
DR PDB; 2OI4; X-ray; 2.20 A; X=1-313.
DR PDB; 2XIX; X-ray; 2.40 A; A=14-313.
DR PDB; 2XIY; X-ray; 2.20 A; A=14-313.
DR PDB; 2XIZ; X-ray; 2.21 A; A=14-313.
DR PDB; 2XJ0; X-ray; 3.10 A; A=14-313.
DR PDB; 2XJ1; X-ray; 2.13 A; A=14-313.
DR PDB; 2XJ2; X-ray; 2.20 A; A=14-313.
DR PDB; 3A99; X-ray; 1.60 A; A=15-313.
DR PDB; 3BGP; X-ray; 2.80 A; A=1-313.
DR PDB; 3BGQ; X-ray; 2.00 A; A=1-313.
DR PDB; 3BGZ; X-ray; 2.40 A; A=1-313.
DR PDB; 3BWF; X-ray; 2.35 A; A=1-313.
DR PDB; 3C4E; X-ray; 1.98 A; A/B/C/D=33-305.
DR PDB; 3CXW; X-ray; 2.10 A; A=1-313.
DR PDB; 3CY2; X-ray; 2.01 A; A=1-313.
DR PDB; 3CY3; X-ray; 2.15 A; A=1-313.
DR PDB; 3DCV; X-ray; 2.70 A; A=2-313.
DR PDB; 3F2A; X-ray; 1.90 A; A=14-313.
DR PDB; 3JPV; X-ray; 2.35 A; A=1-312.
DR PDB; 3JXW; X-ray; 2.80 A; A=29-313.
DR PDB; 3JY0; X-ray; 2.40 A; A=29-313.
DR PDB; 3JYA; X-ray; 2.10 A; A=29-313.
DR PDB; 3MA3; X-ray; 2.30 A; A=2-312.
DR PDB; 3QF9; X-ray; 2.20 A; A=1-312.
DR PDB; 3R00; X-ray; 2.10 A; A=29-313.
DR PDB; 3R01; X-ray; 2.60 A; A=29-313.
DR PDB; 3R02; X-ray; 1.95 A; A=29-313.
DR PDB; 3R04; X-ray; 1.70 A; A=29-313.
DR PDB; 3T9I; X-ray; 2.60 A; A=2-313.
DR PDB; 3UIX; X-ray; 2.20 A; A=29-313.
DR PDB; 3UMW; X-ray; 2.08 A; A=29-313.
DR PDB; 3UMX; X-ray; 2.55 A; A=29-313.
DR PDB; 3VBQ; X-ray; 1.85 A; A=29-313.
DR PDB; 3VBT; X-ray; 2.23 A; A=29-313.
DR PDB; 3VBV; X-ray; 2.08 A; A=29-313.
DR PDB; 3VBW; X-ray; 2.48 A; A=29-313.
DR PDB; 3VBX; X-ray; 2.03 A; A=29-313.
DR PDB; 3VBY; X-ray; 2.27 A; A=29-313.
DR PDB; 3VC4; X-ray; 2.23 A; A=29-313.
DR PDB; 3WE8; X-ray; 1.95 A; A=33-305.
DR PDB; 4A7C; X-ray; 2.30 A; A=30-313.
DR PDB; 4ALU; X-ray; 2.60 A; A=2-313.
DR PDB; 4ALV; X-ray; 2.59 A; A=2-313.
DR PDB; 4ALW; X-ray; 1.92 A; A=2-313.
DR PDB; 4AS0; X-ray; 2.30 A; A=33-305.
DR PDB; 4BZN; X-ray; 1.90 A; A=2-313.
DR PDB; 4BZO; X-ray; 2.10 A; A=2-313.
DR PDB; 4DTK; X-ray; 1.86 A; A=30-305.
DR PDB; 4ENX; X-ray; 2.80 A; A=29-313.
DR PDB; 4ENY; X-ray; 2.80 A; A=29-313.
DR PDB; 4GW8; X-ray; 2.00 A; A=1-312.
DR PDB; 4I41; X-ray; 2.70 A; A=29-305.
DR PDB; 4IAA; X-ray; 2.85 A; A=29-313.
DR PDB; 4JX3; X-ray; 2.50 A; A=1-313.
DR PDB; 4JX7; X-ray; 2.40 A; A=1-313.
DR PDB; 4K0Y; X-ray; 1.95 A; A=33-306.
DR PDB; 4K18; X-ray; 2.05 A; A=32-308.
DR PDB; 4K1B; X-ray; 2.08 A; A=33-305.
DR PDB; 4LL5; X-ray; 2.00 A; A=29-313.
DR PDB; 4LM5; X-ray; 2.25 A; A=29-313.
DR PDB; 4LMU; X-ray; 2.38 A; A=29-313.
DR PDB; 4MBI; X-ray; 2.30 A; A=29-313.
DR PDB; 4MBL; X-ray; 2.60 A; A=29-313.
DR PDB; 4MTA; X-ray; 2.20 A; A=28-313.
DR PDB; 4N6Y; X-ray; 2.60 A; A=2-313.
DR PDB; 4N6Z; X-ray; 2.20 A; A=2-313.
DR PDB; 4N70; X-ray; 2.10 A; A=2-313.
DR PDB; 4RBL; X-ray; 2.55 A; A=29-313.
DR PDB; 4RC2; X-ray; 2.10 A; A=29-313.
DR PDB; 4RC3; X-ray; 2.34 A; A=29-313.
DR PDB; 4RC4; X-ray; 2.65 A; A=29-313.
DR PDB; 4RPV; X-ray; 3.05 A; A=1-313.
DR PDB; 4TY1; X-ray; 2.70 A; A=33-305.
DR PDB; 4WRS; X-ray; 2.20 A; A=33-305.
DR PDB; 4WSY; X-ray; 2.30 A; A=33-305.
DR PDB; 4WT6; X-ray; 2.30 A; A=33-305.
DR PDB; 4XH6; X-ray; 2.04 A; A=29-313.
DR PDB; 4XHK; X-ray; 1.90 A; B=1-313.
DR PDB; 5C1Q; X-ray; 3.00 A; B=29-313.
DR PDB; 5DGZ; X-ray; 2.50 A; A=29-313.
DR PDB; 5DHJ; X-ray; 2.46 A; A=29-313.
DR PDB; 5DIA; X-ray; 1.96 A; A=29-313.
DR PDB; 5DWR; X-ray; 2.00 A; A=2-313.
DR PDB; 5EOL; X-ray; 2.20 A; A=33-305.
DR PDB; 5IIS; X-ray; 2.10 A; A=32-308.
DR PDB; 5IPJ; X-ray; 2.10 A; A=33-305.
DR PDB; 5KCX; X-ray; 2.20 A; A=29-313.
DR PDB; 5KGD; X-ray; 1.98 A; A=30-305.
DR PDB; 5KGE; X-ray; 2.23 A; A=30-305.
DR PDB; 5KGG; X-ray; 1.95 A; A=30-305.
DR PDB; 5KGI; X-ray; 2.13 A; A=30-305.
DR PDB; 5KGK; X-ray; 2.66 A; A=30-305.
DR PDB; 5KZI; X-ray; 2.10 A; A=33-305.
DR PDB; 5MZL; X-ray; 1.96 A; A=1-313.
DR PDB; 5N4N; X-ray; 2.09 A; A=1-313.
DR PDB; 5N4O; X-ray; 2.22 A; A=1-313.
DR PDB; 5N4R; X-ray; 2.13 A; A=1-313.
DR PDB; 5N4U; X-ray; 2.20 A; A=1-313.
DR PDB; 5N4V; X-ray; 1.85 A; A=1-313.
DR PDB; 5N4X; X-ray; 2.20 A; A=1-313.
DR PDB; 5N4Y; X-ray; 2.56 A; A=1-313.
DR PDB; 5N4Z; X-ray; 2.26 A; A=1-313.
DR PDB; 5N50; X-ray; 1.92 A; A=1-313.
DR PDB; 5N51; X-ray; 2.12 A; A=1-313.
DR PDB; 5N52; X-ray; 2.25 A; A=1-313.
DR PDB; 5N5L; X-ray; 1.97 A; A=1-313.
DR PDB; 5N5M; X-ray; 2.21 A; A=1-313.
DR PDB; 5NDT; X-ray; 1.99 A; A=1-313.
DR PDB; 5O11; X-ray; 2.40 A; A=29-313.
DR PDB; 5O12; X-ray; 2.40 A; A=29-313.
DR PDB; 5O13; X-ray; 2.44 A; A=29-313.
DR PDB; 5TEL; X-ray; 2.21 A; A=33-306.
DR PDB; 5TEX; X-ray; 2.15 A; A=33-306.
DR PDB; 5TOE; X-ray; 2.30 A; A=34-306.
DR PDB; 5TUR; X-ray; 2.95 A; A=1-313.
DR PDB; 5V80; X-ray; 2.25 A; A=29-313.
DR PDB; 5V82; X-ray; 1.89 A; A=29-313.
DR PDB; 5VUA; X-ray; 2.20 A; B=29-313.
DR PDB; 5VUB; X-ray; 2.00 A; B=29-313.
DR PDB; 5VUC; X-ray; 2.00 A; B=29-313.
DR PDB; 6AYD; X-ray; 3.00 A; A=1-312.
DR PDB; 6BSK; X-ray; 2.57 A; A=30-305.
DR PDB; 6KZI; X-ray; 2.80 A; A=29-313.
DR PDB; 6L11; X-ray; 2.05 A; A=29-313.
DR PDB; 6L12; X-ray; 1.87 A; A=29-313.
DR PDB; 6L13; X-ray; 2.24 A; A=29-313.
DR PDB; 6L14; X-ray; 1.95 A; A=29-313.
DR PDB; 6L15; X-ray; 2.60 A; A=29-313.
DR PDB; 6L16; X-ray; 2.10 A; A=29-313.
DR PDB; 6L17; X-ray; 1.75 A; A=29-313.
DR PDB; 6MT0; X-ray; 2.20 A; A=33-305.
DR PDB; 6NO8; X-ray; 2.38 A; A=33-305.
DR PDB; 6NO9; X-ray; 1.71 A; A=33-305.
DR PDB; 6PCW; X-ray; 2.20 A; A=1-312.
DR PDB; 6PDI; X-ray; 1.85 A; A=1-312.
DR PDB; 6PDN; X-ray; 2.40 A; A=1-312.
DR PDB; 6PDO; X-ray; 2.40 A; A=1-312.
DR PDB; 6PDP; X-ray; 2.50 A; A=1-312.
DR PDB; 6QXK; X-ray; 2.10 A; B=1-312.
DR PDB; 6VRU; X-ray; 2.07 A; A=33-306.
DR PDB; 6VRV; X-ray; 1.74 A; A=33-306.
DR PDB; 6YKD; X-ray; 1.86 A; A=1-313.
DR PDB; 7OOV; X-ray; 1.96 A; A=1-312.
DR PDB; 7OOW; X-ray; 1.95 A; A=1-312.
DR PDB; 7OOX; X-ray; 1.97 A; A=1-312.
DR PDBsum; 1XQZ; -.
DR PDBsum; 1XR1; -.
DR PDBsum; 1XWS; -.
DR PDBsum; 1YHS; -.
DR PDBsum; 1YI3; -.
DR PDBsum; 1YI4; -.
DR PDBsum; 1YWV; -.
DR PDBsum; 1YXS; -.
DR PDBsum; 1YXT; -.
DR PDBsum; 1YXU; -.
DR PDBsum; 1YXV; -.
DR PDBsum; 1YXX; -.
DR PDBsum; 2BIK; -.
DR PDBsum; 2BIL; -.
DR PDBsum; 2BZH; -.
DR PDBsum; 2BZI; -.
DR PDBsum; 2BZJ; -.
DR PDBsum; 2BZK; -.
DR PDBsum; 2C3I; -.
DR PDBsum; 2J2I; -.
DR PDBsum; 2O3P; -.
DR PDBsum; 2O63; -.
DR PDBsum; 2O64; -.
DR PDBsum; 2O65; -.
DR PDBsum; 2OBJ; -.
DR PDBsum; 2OI4; -.
DR PDBsum; 2XIX; -.
DR PDBsum; 2XIY; -.
DR PDBsum; 2XIZ; -.
DR PDBsum; 2XJ0; -.
DR PDBsum; 2XJ1; -.
DR PDBsum; 2XJ2; -.
DR PDBsum; 3A99; -.
DR PDBsum; 3BGP; -.
DR PDBsum; 3BGQ; -.
DR PDBsum; 3BGZ; -.
DR PDBsum; 3BWF; -.
DR PDBsum; 3C4E; -.
DR PDBsum; 3CXW; -.
DR PDBsum; 3CY2; -.
DR PDBsum; 3CY3; -.
DR PDBsum; 3DCV; -.
DR PDBsum; 3F2A; -.
DR PDBsum; 3JPV; -.
DR PDBsum; 3JXW; -.
DR PDBsum; 3JY0; -.
DR PDBsum; 3JYA; -.
DR PDBsum; 3MA3; -.
DR PDBsum; 3QF9; -.
DR PDBsum; 3R00; -.
DR PDBsum; 3R01; -.
DR PDBsum; 3R02; -.
DR PDBsum; 3R04; -.
DR PDBsum; 3T9I; -.
DR PDBsum; 3UIX; -.
DR PDBsum; 3UMW; -.
DR PDBsum; 3UMX; -.
DR PDBsum; 3VBQ; -.
DR PDBsum; 3VBT; -.
DR PDBsum; 3VBV; -.
DR PDBsum; 3VBW; -.
DR PDBsum; 3VBX; -.
DR PDBsum; 3VBY; -.
DR PDBsum; 3VC4; -.
DR PDBsum; 3WE8; -.
DR PDBsum; 4A7C; -.
DR PDBsum; 4ALU; -.
DR PDBsum; 4ALV; -.
DR PDBsum; 4ALW; -.
DR PDBsum; 4AS0; -.
DR PDBsum; 4BZN; -.
DR PDBsum; 4BZO; -.
DR PDBsum; 4DTK; -.
DR PDBsum; 4ENX; -.
DR PDBsum; 4ENY; -.
DR PDBsum; 4GW8; -.
DR PDBsum; 4I41; -.
DR PDBsum; 4IAA; -.
DR PDBsum; 4JX3; -.
DR PDBsum; 4JX7; -.
DR PDBsum; 4K0Y; -.
DR PDBsum; 4K18; -.
DR PDBsum; 4K1B; -.
DR PDBsum; 4LL5; -.
DR PDBsum; 4LM5; -.
DR PDBsum; 4LMU; -.
DR PDBsum; 4MBI; -.
DR PDBsum; 4MBL; -.
DR PDBsum; 4MTA; -.
DR PDBsum; 4N6Y; -.
DR PDBsum; 4N6Z; -.
DR PDBsum; 4N70; -.
DR PDBsum; 4RBL; -.
DR PDBsum; 4RC2; -.
DR PDBsum; 4RC3; -.
DR PDBsum; 4RC4; -.
DR PDBsum; 4RPV; -.
DR PDBsum; 4TY1; -.
DR PDBsum; 4WRS; -.
DR PDBsum; 4WSY; -.
DR PDBsum; 4WT6; -.
DR PDBsum; 4XH6; -.
DR PDBsum; 4XHK; -.
DR PDBsum; 5C1Q; -.
DR PDBsum; 5DGZ; -.
DR PDBsum; 5DHJ; -.
DR PDBsum; 5DIA; -.
DR PDBsum; 5DWR; -.
DR PDBsum; 5EOL; -.
DR PDBsum; 5IIS; -.
DR PDBsum; 5IPJ; -.
DR PDBsum; 5KCX; -.
DR PDBsum; 5KGD; -.
DR PDBsum; 5KGE; -.
DR PDBsum; 5KGG; -.
DR PDBsum; 5KGI; -.
DR PDBsum; 5KGK; -.
DR PDBsum; 5KZI; -.
DR PDBsum; 5MZL; -.
DR PDBsum; 5N4N; -.
DR PDBsum; 5N4O; -.
DR PDBsum; 5N4R; -.
DR PDBsum; 5N4U; -.
DR PDBsum; 5N4V; -.
DR PDBsum; 5N4X; -.
DR PDBsum; 5N4Y; -.
DR PDBsum; 5N4Z; -.
DR PDBsum; 5N50; -.
DR PDBsum; 5N51; -.
DR PDBsum; 5N52; -.
DR PDBsum; 5N5L; -.
DR PDBsum; 5N5M; -.
DR PDBsum; 5NDT; -.
DR PDBsum; 5O11; -.
DR PDBsum; 5O12; -.
DR PDBsum; 5O13; -.
DR PDBsum; 5TEL; -.
DR PDBsum; 5TEX; -.
DR PDBsum; 5TOE; -.
DR PDBsum; 5TUR; -.
DR PDBsum; 5V80; -.
DR PDBsum; 5V82; -.
DR PDBsum; 5VUA; -.
DR PDBsum; 5VUB; -.
DR PDBsum; 5VUC; -.
DR PDBsum; 6AYD; -.
DR PDBsum; 6BSK; -.
DR PDBsum; 6KZI; -.
DR PDBsum; 6L11; -.
DR PDBsum; 6L12; -.
DR PDBsum; 6L13; -.
DR PDBsum; 6L14; -.
DR PDBsum; 6L15; -.
DR PDBsum; 6L16; -.
DR PDBsum; 6L17; -.
DR PDBsum; 6MT0; -.
DR PDBsum; 6NO8; -.
DR PDBsum; 6NO9; -.
DR PDBsum; 6PCW; -.
DR PDBsum; 6PDI; -.
DR PDBsum; 6PDN; -.
DR PDBsum; 6PDO; -.
DR PDBsum; 6PDP; -.
DR PDBsum; 6QXK; -.
DR PDBsum; 6VRU; -.
DR PDBsum; 6VRV; -.
DR PDBsum; 6YKD; -.
DR PDBsum; 7OOV; -.
DR PDBsum; 7OOW; -.
DR PDBsum; 7OOX; -.
DR AlphaFoldDB; P11309; -.
DR SMR; P11309; -.
DR BioGRID; 111310; 66.
DR IntAct; P11309; 38.
DR MINT; P11309; -.
DR STRING; 9606.ENSP00000362608; -.
DR BindingDB; P11309; -.
DR ChEMBL; CHEMBL2147; -.
DR DrugBank; DB08022; (2S)-1,3-benzothiazol-2-yl{2-[(2-pyridin-3-ylethyl)amino]pyrimidin-4-yl}ethanenitrile.
DR DrugBank; DB03650; (3e)-3-[(4-Hydroxyphenyl)Imino]-1h-Indol-2(3h)-One.
DR DrugBank; DB07242; (4R)-7,8-dichloro-1',9-dimethyl-1-oxo-1,2,4,9-tetrahydrospiro[beta-carboline-3,4'-piperidine]-4-carbonitrile.
DR DrugBank; DB08166; (4R)-7-chloro-9-methyl-1-oxo-1,2,4,9-tetrahydrospiro[beta-carboline-3,4'-piperidine]-4-carbonitrile.
DR DrugBank; DB08709; 2,3-diphenyl-1H-indole-7-carboxylic acid.
DR DrugBank; DB01754; 3,4-Dihydroxy-1-Methylquinolin-2(1h)-One.
DR DrugBank; DB07151; 4-(4-hydroxy-3-methylphenyl)-6-phenylpyrimidin-2(5H)-one.
DR DrugBank; DB08707; 4-[3-(4-chlorophenyl)-2,1-benzisoxazol-5-yl]pyrimidin-2-amine.
DR DrugBank; DB08705; 6-(5-BROMO-2-HYDROXYPHENYL)-2-OXO-4-PHENYL-1,2-DIHYDROPYRIDINE-3-CARBONITRILE.
DR DrugBank; DB03777; Bisindolylmaleimide I.
DR DrugBank; DB04522; Dexfosfoserine.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB03366; Imidazole.
DR DrugBank; DB04715; IMIDAZOPYRIDAZIN 1.
DR DrugBank; DB02656; LY-294002.
DR DrugBank; DB08708; N-cyclohexyl-3-[3-(trifluoromethyl)phenyl][1,2,4]triazolo[4,3-b]pyridazin-6-amine.
DR DrugBank; DB07524; N-phenyl-1H-pyrrolo[2,3-b]pyridin-3-amine.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine.
DR DrugBank; DB02010; Staurosporine.
DR DrugBank; DB08230; Tricetin.
DR DrugCentral; P11309; -.
DR GuidetoPHARMACOLOGY; 2158; -.
DR GlyGen; P11309; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11309; -.
DR PhosphoSitePlus; P11309; -.
DR BioMuta; PIM1; -.
DR DMDM; 83305339; -.
DR EPD; P11309; -.
DR jPOST; P11309; -.
DR MassIVE; P11309; -.
DR MaxQB; P11309; -.
DR PaxDb; P11309; -.
DR PeptideAtlas; P11309; -.
DR PRIDE; P11309; -.
DR ProteomicsDB; 52741; -. [P11309-1]
DR ProteomicsDB; 52742; -. [P11309-2]
DR Antibodypedia; 1207; 727 antibodies from 38 providers.
DR DNASU; 5292; -.
DR Ensembl; ENST00000373509.6; ENSP00000362608.5; ENSG00000137193.14. [P11309-1]
DR GeneID; 5292; -.
DR KEGG; hsa:5292; -.
DR MANE-Select; ENST00000373509.6; ENSP00000362608.5; NM_002648.4; NP_002639.1.
DR UCSC; uc003onk.4; human. [P11309-1]
DR CTD; 5292; -.
DR DisGeNET; 5292; -.
DR GeneCards; PIM1; -.
DR HGNC; HGNC:8986; PIM1.
DR HPA; ENSG00000137193; Tissue enhanced (bone marrow, esophagus).
DR MIM; 164960; gene.
DR neXtProt; NX_P11309; -.
DR OpenTargets; ENSG00000137193; -.
DR PharmGKB; PA33318; -.
DR VEuPathDB; HostDB:ENSG00000137193; -.
DR eggNOG; KOG0583; Eukaryota.
DR GeneTree; ENSGT00940000153394; -.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; P11309; -.
DR OMA; QDIHLEP; -.
DR OrthoDB; 930292at2759; -.
DR PhylomeDB; P11309; -.
DR TreeFam; TF320810; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P11309; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9702518; STAT5 activation downstream of FLT3 ITD mutants.
DR Reactome; R-HSA-9703465; Signaling by FLT3 fusion proteins.
DR SignaLink; P11309; -.
DR SIGNOR; P11309; -.
DR BioGRID-ORCS; 5292; 39 hits in 1115 CRISPR screens.
DR ChiTaRS; PIM1; human.
DR EvolutionaryTrace; P11309; -.
DR GeneWiki; PIM1; -.
DR GenomeRNAi; 5292; -.
DR Pharos; P11309; Tchem.
DR PRO; PR:P11309; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P11309; protein.
DR Bgee; ENSG00000137193; Expressed in lower esophagus mucosa and 177 other tissues.
DR ExpressionAtlas; P11309; baseline and differential.
DR Genevisible; P11309; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit binding; IPI:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:1990748; P:cellular detoxification; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:BHF-UCL.
DR GO; GO:1905062; P:positive regulation of cardioblast proliferation; IDA:BHF-UCL.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:1902033; P:regulation of hematopoietic stem cell proliferation; IEA:Ensembl.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0070561; P:vitamin D receptor signaling pathway; IMP:CACAO.
DR DisProt; DP00322; -.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017348; PIM1/2/3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037993; STPK_Pim-1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Apoptosis; ATP-binding; Cell cycle;
KW Cell membrane; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Ubl conjugation.
FT CHAIN 1..313
FT /note="Serine/threonine-protein kinase pim-1"
FT /id="PRO_0000043349"
FT DOMAIN 38..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15657054,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15657054"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15657054"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15657054"
FT VAR_SEQ 1
FT /note="M -> MPHEPHEPLTPPFSALPDPAGAPSRRQSRQRPQLSSDSPSAFRASRS
FT HSRNATRSHSHSHSPRHSLRHSPGSGSCGSSSGHRPCADILEVGM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16186805"
FT /id="VSP_059829"
FT VARIANT 53
FT /note="Y -> H (in a colorectal adenocarcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041004"
FT VARIANT 124
FT /note="E -> Q (in dbSNP:rs35760989)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041005"
FT VARIANT 135
FT /note="E -> K (in dbSNP:rs200523275)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041006"
FT VARIANT 142
FT /note="E -> D (in dbSNP:rs33989191)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041007"
FT MUTAGEN 68
FT /note="H->Y: Increased kinase activity."
FT /evidence="ECO:0000269|PubMed:15808862"
FT MUTAGEN 81
FT /note="P->S: Decreased kinase activity."
FT /evidence="ECO:0000269|PubMed:15808862"
FT MUTAGEN 82
FT /note="N->K: Decreased kinase activity."
FT /evidence="ECO:0000269|PubMed:15808862"
FT MUTAGEN 193
FT /note="L->F: Decreased kinase activity."
FT /evidence="ECO:0000269|PubMed:15808862"
FT CONFLICT 15..16
FT /note="AP -> RA (in Ref. 2; AAA60089)"
FT /evidence="ECO:0000305"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:7OOX"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:7OOX"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3A99"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3A99"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3C4E"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:3VBQ"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 141..160
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3A99"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:3A99"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4ALW"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 220..237
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 261..270
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3A99"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:3A99"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:3F2A"
SQ SEQUENCE 313 AA; 35686 MW; 35BA76D3668E69A3 CRC64;
MLLSKINSLA HLRAAPCNDL HATKLAPGKE KEPLESQYQV GPLLGSGGFG SVYSGIRVSD
NLPVAIKHVE KDRISDWGEL PNGTRVPMEV VLLKKVSSGF SGVIRLLDWF ERPDSFVLIL
ERPEPVQDLF DFITERGALQ EELARSFFWQ VLEAVRHCHN CGVLHRDIKD ENILIDLNRG
ELKLIDFGSG ALLKDTVYTD FDGTRVYSPP EWIRYHRYHG RSAAVWSLGI LLYDMVCGDI
PFEHDEEIIR GQVFFRQRVS SECQHLIRWC LALRPSDRPT FEEIQNHPWM QDVLLPQETA
EIHLHSLSPG PSK
